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. 2022 Dec 21:13:1086383.
doi: 10.3389/fmicb.2022.1086383. eCollection 2022.

Fiber-1 of serotype 4 fowl adenovirus mediates superinfection resistance against serotype 8b fowl adenovirus

Hao Lu  1   2   3   4 , Yiwen Guo  1   2   3   4 , Zhenqi Xu  1   2   3   4 , Weikang Wang  1   2   3   4 , Mingjun Lian  1   2   3   4 , Tuofan Li  1   2   3   4 , Zhimin Wan  1   2   3   4 , Hongxia Shao  1   2   3   4 , Aijian Qin  1   2   3   4 , Quan Xie  1   2   3   4 , Jianqiang Ye  1   2   3   4
Affiliations

Fiber-1 of serotype 4 fowl adenovirus mediates superinfection resistance against serotype 8b fowl adenovirus

Hao Lu et al. Front Microbiol. .

Abstract

In recent years, hepatitis-hydropericardium syndrome (HHS) and inclusion body hepatitis (IBH) caused by serotype 4 fowl adenovirus (FAdV-4) and serotype 8b fowl adenovirus (FAdV-8b), respectively, are widely prevalent in China, causing huge economic losses to the poultry industry. Numerous studies have revealed the mechanism of the infection and pathogenesis of FAdV-4. However, little is known about the mechanism of infection with FAdV-8b. Among the major structural proteins of fowl adenoviruses, fiber is characterized by the ability to recognize and bind to cellular receptors to mediate the infection of host cells. In this study, through superinfection resistance analysis and an interfering assay, we found that Fiber-1 of FAdV-4, rather than hexon, penton, and fiber of FAdV-8b, conferred efficient superinfection resistance against the infection FAdV-8b in LMH cells. Moreover, truncation analysis depicted that the shaft and knob domains of FAdV-4 Fiber-1 were responsible for the inhibition. However, knockout of the coxsackie and adenovirus receptor (CAR) in LMH cells inhibited the replication of FAdV-8b only at early time points, indicating that CAR might not be the key cell receptor for FAdV-8b. Overall, our findings give novel insights into the infection mechanism of FAdV-8b and provide a new target for the prevention and control of both FAdV-4 and FAdV-8b.

Keywords: CAR; FAdV-8b; Fiber-1 of FAdV-4; IBH; superinfection.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Fiber, hexon, and penton proteins of FAdV-8b were unable to inhibit the infection of FAdV-8b in the superinfection resistance assay. (A) LMH cells transfected with pcDNA3.1-Fiber, pcDNA3.1-Hexon, pcDNA3.1-Penton, and pcDNA3.1 were analyzed by IFA using the chicken sera against FAdV-8b. (B) Supernatants from the LMH cells infected with FAdV-8b at different time points, which were transfected with pcDNA3.1-Fiber, pcDNA3.1-Hexon, pcDNA3.1-Penton, and pcDNA3.1 and titrated with TCID50.
Figure 2
Figure 2
Fiber-1 of FAdV-4 conferred efficient superinfection resistance against FAdV-8b. (A) LMH cells transfected with pcDNA3.1-F1 of FAdV-4 were analyzed by IFA using mAb 3B5 against Fiber-1 of FAdV-4. (B) Supernatants from the LMH cells infected with FAdV-7, FAdV-8a, and FAdV-8b at different time points, which were transfected with pcDNA3.1-F1 and pcDNA3.1 and titrated with TCID50. (C) LMH cells infected with FAdV-7, FAdV-8a, and FAdV-8b at 120 hpi, which were transfected with pcDNA3.1 and pcDNA3.1-F1 and analyzed by Western blot using mAb 1B5 against the hexon protein of FAdVs.
Figure 3
Figure 3
Purified His-Fiber-1 of FAdV-4 efficiently interfered with the infection of FAdV-8b. (A) Supernatants from the LMH cells infected with FAdV-8b at different time points, which were treated with purified; His-Fiber-1 of DAdV-3 and His-Fiber-1 of FAdV-4 were titrated with TCID50. (B) LMH cells infected with FAdV-8b, which were treated with purified; His-Fiber-1 of DAdV-3 and His-Fiber-1 of FAdV-4 were analyzed using mAb 1B5 against the hexon protein of FAdVs and mAb 4D9 against the fiber protein of FAdV-8b by Western blot.
Figure 4
Figure 4
The shaft and knob domains of FAdV-4 Fiber-1 contributed to the superinfection resistance against FAdV-8b. (A) Expression of the different truncated Fiber-1 of FAdV-4 in LMH cells; pcDNA3.1-F1-Tail-Flag, pcDNA3.1-F1-Shaft-Flag, pcDNA3.1-F1-Knob-Flag, pcDNA3.1-F1-Tail+Shaft-Flag, pcDNA3.1-F1-Shaft+Knob-Flag, and pcDNA3.1 were transfected into the LMH cells and examined by IFA using mAb against flag. (B) Supernatants from the LMH cells infected with FAdV-8b at different time points, which were transfected with pcDNA3.1-F1, pcDNA3.1-F1-Tail-Flag, pcDNA3.1-F1-Shaft-Flag, pcDNA3.1-F1-Knob-Flag, pcDNA3.1-F1-Tail+Shaft-Flag, pcDNA3.1-F1-Shaft+Knob-Flag, and pcDNA3.1 and titrated with TCID50. (C) LMH cells infected with FAdV-8b at 120 hpi, which were transfected with pcDNA3.1-F1, pcDNA3.1-F1-Tail-Flag, pcDNA3.1-F1-Shaft-Flag, pcDNA3.1-F1-Knob-Flag, pcDNA3.1-F1-Tail+Shaft-Flag, pcDNA3.1-F1-Shaft+Knob-Flag, and pcDNA3.1 and analyzed using mAb 1B5 against the hexon protein of FAdVs and mAb 4D9 against the fiber protein of FAdV-8b by Western blot.
Figure 5
Figure 5
Knockout of the CAR gene in LMH cells affected the replication of FAdV-8b. (A) The expression of CAR in CAR-KO LMH cells was examined using polyclonal antibodies against CAR through Western blot. (B) Supernatants collected from CAR-KO LMH cells and WT LMH cells infected with FAdV-8b at different time points were titrated with TCID50. (C) CAR-KO LMH cells and WT LMH cells infected with FAdV-8b at 48 hpi were analyzed using mAb 1B5 against the hexon protein of FAdVs by Western blot.
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References

    1. Benko M., Aoki K., Arnberg N., Davison A. J., Echavarria M., Hess M., et al. . (2022). ICTV virus taxonomy profile: adenoviridae 2022. J. Gen. Virol. 103, 1721. 10.1099./jgv.0.001721 - DOI - PMC - PubMed
    1. Changjing L., Haiying L., Dongdong W., Jingjing W., Youming W., Shouchun W., et al. . (2016). Characterization of fowl adenoviruses isolated between 2007 and 2014 in China. Vet. Microbiol. 197, 62–67. 10.1016/j.vetmic.11005 - DOI - PubMed
    1. Chen L., Yin L., Zhou Q., Peng P., Du Y., Liu L., et al. . (2019). Epidemiological investigation of fowl adenovirus infections in poultry in China during 2015–2018. BMC Vet. Res. 15, 271. 10.1186/s12917-019-1969-7 - DOI - PMC - PubMed
    1. De Luca Schachner, C., Mitra A., Heidl T., Liebhart S., Hess D., et al. . (2020). Fowl adenovirus (FAdV) fiber-based vaccine against inclusion body hepatitis (IBH) provides type-specific protection guided by humoral immunity and regulation of B and T cell response. Vet. Res. 51, 143. 10.1186/s13567-020-00869-8 - DOI - PMC - PubMed
    1. Garmyn A., Bosseler L., Braeckmans D., Van Erum J., Verlinden M. (2018). Adenoviral gizzard erosions in two belgian broiler farms. Avian. Dis. 62, 322–325. 10.1637/11826-030918-Case.1 - DOI - PubMed

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